RFXK_MOUSE
ID RFXK_MOUSE Reviewed; 269 AA.
AC Q9Z205;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=DNA-binding protein RFXANK;
DE AltName: Full=Ankyrin repeat-containing adapter protein Tvl-1;
DE AltName: Full=Regulatory factor X subunit B;
DE Short=RFX-B;
DE AltName: Full=Regulatory factor X-associated ankyrin-containing protein;
GN Name=Rfxank; Synonyms=Rfxb, Tvl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=9806546; DOI=10.1038/3081;
RA Masternak K., Barras E., Zufferey M., Conrad B., Corthals G., Aebersold R.,
RA Sanchez J.-C., Hochstrasser D.F., Mach B., Reith W.;
RT "A gene encoding a novel RFX-associated transactivator is mutated in the
RT majority of MHC class II deficiency patients.";
RL Nat. Genet. 20:273-277(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH RAF1, SUBUNIT, DOMAIN, AND PHOSPHORYLATION.
RC TISSUE=T-cell;
RX PubMed=10329666; DOI=10.1074/jbc.274.21.14706;
RA Lin J.-H., Makris A., McMahon C., Bear S.E., Patriotis C., Prasad V.R.,
RA Brent R., Golemis E.A., Tsichlis P.N.;
RT "The ankyrin repeat-containing adaptor protein tvl-1 is a novel substrate
RT and regulator of raf-1.";
RL J. Biol. Chem. 274:14706-14715(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Activates transcription from class II MHC promoters.
CC Activation requires the activity of the MHC class II
CC transactivator/CIITA. May regulate other genes in the cell. RFX binds
CC the X1 box of MHC-II promoters (By similarity). May also potentiate the
CC activation of RAF1 (PubMed:10329666). {ECO:0000250|UniProtKB:O14593,
CC ECO:0000269|PubMed:10329666}.
CC -!- SUBUNIT: Forms homodimers (PubMed:10329666). The RFX heterotetrameric
CC complex consists of 2 molecules of RFX5 and one each of RFXAP and RFX-
CC B/RFXANK; with each subunit representing a separate complementation
CC group. Interacts (via ankyrin repeats) with RFX5 (via PxLPxI/L motif);
CC the interaction is direct. RFX forms cooperative DNA binding complexes
CC with X2BP and CBF/NF-Y. RFX associates with CIITA to form an active
CC transcriptional complex (By similarity). Interacts with RAF1
CC (PubMed:10329666). Interacts with RFX7 (By similarity).
CC {ECO:0000250|UniProtKB:O14593, ECO:0000269|PubMed:10329666}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10329666}. Nucleus
CC {ECO:0000269|PubMed:10329666}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q9Z205-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q9Z205-2; Sequence=VSP_000285;
CC -!- TISSUE SPECIFICITY: Expressed primarily in thymus, lung and testis.
CC -!- DOMAIN: Interacts with RAF-1 via its C-terminal ankyrin repeat domain.
CC The same domain also mediates its homodimerization (PubMed:10329666).
CC The third ankyrin repeat is required for association with the two other
CC RFX subunits; RFX5 and RFXAP. The three central ANK repeats mediate
CC binding to the PxLPxI/L motif of RFX5 (By similarity).
CC {ECO:0000250|UniProtKB:O14593, ECO:0000269|PubMed:10329666}.
CC -!- PTM: Phosphorylated by RAF1. {ECO:0000269|PubMed:10329666}.
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DR EMBL; AF094761; AAC69884.1; -; mRNA.
DR EMBL; AF123704; AAD24798.1; -; mRNA.
DR EMBL; BC010971; AAH10971.1; -; mRNA.
DR CCDS; CCDS22360.1; -. [Q9Z205-1]
DR CCDS; CCDS85552.1; -. [Q9Z205-2]
DR RefSeq; NP_001020760.1; NM_001025589.1. [Q9Z205-2]
DR RefSeq; NP_035396.1; NM_011266.2. [Q9Z205-1]
DR AlphaFoldDB; Q9Z205; -.
DR SMR; Q9Z205; -.
DR BioGRID; 202875; 7.
DR IntAct; Q9Z205; 2.
DR STRING; 10090.ENSMUSP00000075140; -.
DR PhosphoSitePlus; Q9Z205; -.
DR EPD; Q9Z205; -.
DR MaxQB; Q9Z205; -.
DR PaxDb; Q9Z205; -.
DR PRIDE; Q9Z205; -.
DR ProteomicsDB; 255317; -. [Q9Z205-1]
DR ProteomicsDB; 255318; -. [Q9Z205-2]
DR Antibodypedia; 15290; 356 antibodies from 21 providers.
DR DNASU; 19727; -.
DR Ensembl; ENSMUST00000075724; ENSMUSP00000075140; ENSMUSG00000036120. [Q9Z205-2]
DR Ensembl; ENSMUST00000212320; ENSMUSP00000148739; ENSMUSG00000036120. [Q9Z205-1]
DR GeneID; 19727; -.
DR KEGG; mmu:19727; -.
DR UCSC; uc009lyt.1; mouse. [Q9Z205-1]
DR CTD; 8625; -.
DR MGI; MGI:1333865; Rfxank.
DR VEuPathDB; HostDB:ENSMUSG00000036120; -.
DR eggNOG; KOG0502; Eukaryota.
DR GeneTree; ENSGT00940000160753; -.
DR HOGENOM; CLU_000134_23_0_1; -.
DR InParanoid; Q9Z205; -.
DR OMA; ADSGHMD; -.
DR PhylomeDB; Q9Z205; -.
DR TreeFam; TF333112; -.
DR BioGRID-ORCS; 19727; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Rfxank; mouse.
DR PRO; PR:Q9Z205; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9Z205; protein.
DR Bgee; ENSMUSG00000036120; Expressed in granulocyte and 266 other tissues.
DR ExpressionAtlas; Q9Z205; baseline and differential.
DR Genevisible; Q9Z205; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; IPI:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017362; DNA-bd_RFXANK.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13606; Ank_3; 1.
DR PIRSF; PIRSF038034; DNA-binding_RFXANK; 1.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; ANK repeat; Cytoplasm; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..269
FT /note="DNA-binding protein RFXANK"
FT /id="PRO_0000067050"
FT REPEAT 88..127
FT /note="ANK 1"
FT REPEAT 132..161
FT /note="ANK 2"
FT REPEAT 165..194
FT /note="ANK 3"
FT REPEAT 198..227
FT /note="ANK 4"
FT REPEAT 231..260
FT /note="ANK 5"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 112..121
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_000285"
SQ SEQUENCE 269 AA; 29232 MW; 5713F335DC669E87 CRC64;
MEPTQVAENL VPNQQPPVPD LEDPEDTRDE SPENSDTVVL SLFPCTPDAV NPEADASASS
LQGSFLKHST TLTNRQRGNE VSALPATLDS LSIHQLAAQG ELSQLKDHLR KGACPACTCL
SGNNLINKPD ERGFTPLIWA SAFGEIETVR FLLDWGADPH ILAKERESAL SLASMGGYTD
IVRLLLDRDV DINIYDWNGG TPLLYAVRGN HVKCVEALLA RGADLTTEAD SGYTPMDLAV
ALGYRKVQQV MESHILRLFQ STLGPVDPE
